Welcome to Medical News Today

Healthline Media, Inc. would like to process and share personal data (e.g., mobile ad id) and data about your use of our site (e.g., content interests) with our third party partners (see a current list) using cookies and similar automatic collection tools in order to a) personalize content and/or offers on our site or other sites, b) communicate with you upon request, and/or c) for additional reasons upon notice and, when applicable, with your consent.

Healthline Media, Inc. is based in and operates this site from the United States. Any data you provide will be primarily stored and processed in the United States, pursuant to the laws of the United States, which may provide lesser privacy protections than European Economic Area countries.

By clicking “accept” below, you acknowledge and grant your consent for these activities unless and until you withdraw your consent using our rights request form. Learn more in our Privacy Policy.

Please accept our privacy terms

We use cookies and similar technologies to improve your browsing experience, personalize content and offers, show targeted ads, analyze traffic, and better understand you. We may share your information with third-party partners for marketing purposes. To learn more and make choices about data use, visit our Advertising Policy and Privacy Policy. By clicking “Accept and Continue” below, (1) you consent to these activities unless and until you withdraw your consent using our rights request form, and (2) you consent to allow your data to be transferred, processed, and stored in the United States.

The joy of a juicy hamburger could make a comeback thanks a new discovery by scientists from the University of Kentucky. In a new research report in the December 2010 print issue of The FASEB Journal, scientists found that a protein our body uses to break up blood clots speeds up the progress of prion diseases. This substance, called plasminogen, is a new drug target for prion diseases in both humans and animals.

"I hope that our study will aid in developing therapy for prion diseases, which will ultimately improve the quality of life of patients suffering from prion diseases," said Chongsuk Ryou, Ph.D., a researcher involved in the work from the University of Kentucky in Lexington. "Since prion diseases can lay undetected for decades, delaying the ability of the disease-associated prion protein to replicate by targeting the cofactor of the process could be a monumental implication for treatment."

To make this discovery, the researchers used simple test tube reactions to multiply disease-associated prion proteins. The reactions were conducted in the presence or absence of plasminogen. They found that the natural replication of the prions was stimulated by plasminogen in both human and animal cells.

"Rogue prions are one of nature's most interesting, deadly and least understood biological freakshows," said Gerald Weissmann, M.D., Editor-in-Chief of The FASEB Journal. "They are neither virus nor bacteria, but they kill or harm you just the same. By showing how prions hijack our own clot-busting machinery, this work points to a new target for anti-prion therapy."

According to the U.S. National Institute of Allergy and Infectious Diseases, prion diseases are a related group of rare, fatal brain diseases that affect animals and humans. The diseases are characterized by certain misshapen protein molecules that appear in brain tissue. Normal forms of these prion protein molecules reside on the surface of many types of cells, including brain cells, but scientists do not understand what normal prion protein does. On the other hand, scientists believe that abnormal prion protein, which clumps together and accumulates in brain tissue, is the likely cause of the brain damage that occurs. Scientists do not have a good understanding of what causes the normal prion protein to take on the misshapen abnormal form. Prion diseases are also known as transmissible spongiform encephalopathies, and include bovine spongiform encephalopathy ("mad cow" disease) in cattle; Creutzfeldt-Jakob disease in humans; scrapie in sheep; and chronic wasting disease in deer and elk. These proteins may be spread through certain types of contact with infected tissue, body fluids, and possibly, contaminated medical instruments.

2018 Healthline Media UK Ltd. All rights reserved. MNT is the registered trade mark of Healthline Media. Any medical information published on this website is not intended as a substitute for informed medical advice and you should not take any action before consulting with a healthcare professional.